METE_CHLRE
ID METE_CHLRE Reviewed; 814 AA.
AC Q39586;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase;
DE EC=2.1.1.14;
DE AltName: Full=Cobalamin-independent methionine synthase;
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=21gr / CC-1690;
RX PubMed=8616221; DOI=10.1007/bf00020465;
RA Kurvari V., Qian F., Snell W.J.;
RT "Increased transcript levels of a methionine synthase during adhesion-
RT induced activation of Chlamydomonas reinhardtii gametes.";
RL Plant Mol. Biol. 29:1235-1252(1995).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000305}.
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DR EMBL; U36197; AAC49178.1; -; mRNA.
DR PIR; S65083; S65083.
DR AlphaFoldDB; Q39586; -.
DR SMR; Q39586; -.
DR STRING; 3055.EDO96787; -.
DR PRIDE; Q39586; -.
DR ProMEX; Q39586; -.
DR eggNOG; KOG2263; Eukaryota.
DR UniPathway; UPA00051; UER00082.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
DR InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Transferase; Zinc.
FT CHAIN 1..814
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098701"
FT ACT_SITE 708
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 19
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 110
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 445..447
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 445..447
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 498
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 498
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 503
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 526
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 529..530
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 575
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 613
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 613
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
SQ SEQUENCE 814 AA; 86502 MW; 4D6704D1C446EA72 CRC64;
MLSTTTIGFP RIGNQRQLKF AMESYFKGDS GEAELLAVAH KVQSDAWALQ KAAGIAVIGL
DGTLYDQVLD TITWLGAIPP RFKHLSGLQR YYAMARGGAA LDMSKFFDTN YHYLVPELGP
DVLGPATAGP PLQPDFSGPL DKLARGQAVV GRDGAVPILI GPVTFVSLSR GCELPLDQAV
ARLLPTYCAL LQQLAAAGAP EVQLHEPVLA TSEGTGMPTE FETAYAQMAQ AAGSVPLHLV
TYYDDLGAAY PWAVQLPVAA VTLDFLGPPG AAVPSQTLAL LQQHGFPADK RLGAGVVDGR
SVWKDDGTAV ALLRALLDTG AVSSDRLVVT SSAPLQHLPY DLGLELEAPK TPEATAPAAR
AGRPPGFAKQ KVEEIVSVAR LAASPQPPLL QLVMAPWCSC SGCSRARAWR TTPPTSRLSG
SAAKPYDVRA RDEQLQLAAF PTTTIGSFPQ TAEVRRLRQQ LKSGRLTQAE YEGLIAGHIA
HAVGVQEALG IDVLVHGEAE RTDMVEYFGM QLGGMLFTRA GWVQSYGSRC VRPPLVVDDI
TYRGPSTCWE YKVAIPTAAQ PVKGLLTGPV TILNWSFPRK DISRAAQAMQ LGLALRQEVA
ALEAAGCTII QVDDPALREG LPLNGERWAS YLSWAVDAFR LCTGVAAAGT QVVTHLCYSD
FQDILPAIDR MDADVLTIEN SRSDKPMMAA LAAAGYGRDI GPGVYDVHSP VVPSVEFIKS
RIRSFVDSGI LSGRYDRIWV NPDCGLKTRG WPETIAALAN MVEAAAQARA ELQLAGGAAV
APVTGGVEAA GKGGAGQCRR NQPLRGLLPL SCLP
